about
The target spectrum of SdsR small RNA in SalmonellaDEAD-box RNA helicase Dbp4 is required for small-subunit processome formation and function.Nucleic acid chaperone activity associated with the arginine-rich domain of human hepatitis B virus core protein.Computational identification of biologically functional non-hairpin GC-helices in human Argonaute mRNA.Co-regulated expression of alpha and beta mRNAs encoding HLA-DR surface heterodimers is mediated by the MHCII RNA operonSite-selective probing of cTAR destabilization highlights the necessary plasticity of the HIV-1 nucleocapsid protein to chaperone the first strand transfer.Identifying proteins that bind to specific RNAs - focus on simple repeat expansion diseases.Dynamic interactions of the HIV-1 Tat with nucleic acids are critical for Tat activity in reverse transcription.Dissecting the oligonucleotide binding properties of a disordered chaperone protein using surface plasmon resonance.Regulation of mRNA transport, localization and translation in the nervous system of mammals (Review).Functional implication of archaeal homologues of human RNase P protein pair Pop5 and Rpp30.Linker histone H1 stimulates DNA strand exchange between short oligonucleotides retaining high sensitivity to heterology.Functional attributes of evolutionary conserved Arg45 of Wolbachia (Brugia malayi) translation initiation factor-1.Study of E. coli Hfq's RNA annealing acceleration and duplex destabilization activities using substrates with different GC-contents.Proteomic Analysis of Methanonatronarchaeum thermophilum AMET1, a Representative of a Putative New Class of Euryarchaeota, "Methanonatronarchaeia".The DEAD-Box Protein CYT-19 Uses Arginine Residues in Its C-Tail To Tether RNA Substrates.Direct ¹³C-detected NMR experiments for mapping and characterization of hydrogen bonds in RNA.Hfq chaperone brings speed dating to bacterial sRNA
P2860
Q28277062-87AE7B7C-2F70-4191-94CB-A93058D4422FQ30301078-B4857BB1-438A-4CFA-8C42-B8FEEBFF4FC9Q30357029-A024C928-E292-492F-842C-E199C389A20FQ34662743-95F90089-25DE-4EEE-8DF4-9D0D7A1C73ADQ36740824-2E802174-8D74-4084-A11D-509E454911B9Q36814171-620EC481-1E0A-412B-BDAD-8FCEB88704BAQ37401085-E8C20176-8C43-4509-BFD8-AADAFB4D8E0CQ37518644-A0E95B20-B029-45B4-A6E8-91CD9B741F5BQ37528807-AD838CCE-D14C-4284-B128-014F608540D4Q37685418-C55AA326-3C98-46D8-9FAF-BCE557A349FFQ38297783-29FCA22E-A3C7-49EC-8EFA-01CE9851824FQ38330026-5BC40389-DC3F-4029-82CB-BF34CB2FAE52Q38910936-D0BB1637-BACD-49DF-B001-B1E75A71BD4DQ41430016-9331E806-9601-43BB-9667-86EC484EF466Q48184962-DFBBD2B6-E534-4BA9-86FD-58681E14DC14Q48223275-6B29AE3B-C525-472C-9F2C-17FFAAD20B9CQ48245320-3B20C191-C5EC-44F6-8DF3-C16962FA96B0Q57260318-D636FFE8-9C3D-4BF4-A617-6994392E0ED9
P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 13 April 2011
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Transient RNA-protein interactions in RNA folding.
@en
Transient RNA-protein interactions in RNA folding.
@nl
type
label
Transient RNA-protein interactions in RNA folding.
@en
Transient RNA-protein interactions in RNA folding.
@nl
prefLabel
Transient RNA-protein interactions in RNA folding.
@en
Transient RNA-protein interactions in RNA folding.
@nl
P2860
P921
P1433
P1476
Transient RNA-protein interactions in RNA folding.
@en
P2093
Martina Doetsch
Renée Schroeder
P2860
P304
P356
10.1111/J.1742-4658.2011.08094.X
P407
P50
P577
2011-04-13T00:00:00Z
2011-05-01T00:00:00Z